chapter 1
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| molecules move away from water; aggregation occurs | hydrophobic
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| molecules dissolves easily in water. | hydrophilic
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| water breaking macromolecules apart | hydrolysis
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| water forming macromolecules | dehydration
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| high solubility in non- polar organic molecules; low solubility in water | lipids
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| 6 major groups of lipids : | 1. fatty acids 2. triacyglycerols 3. phopholipids 4. glycolipids 5. steroids 6. terpenes
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| Building blocks for most BUT not all complex lipids | fatty acids
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| long chain of carbons truncated at one end by carboxylic acid (-COOH) | FATTY ACID
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| max number of carbons in humans | 24
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| possess only single carbon- carbon bonds | saturated fatty acids
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| possess one or more carbon-carbon double bond | unsaturated fatty acids
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| most fats reach the cell in the form of | fatty acids and NOT triacyglycerols
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| triacyglycerols, phospholipids, and glycolipids are sometimes called | fatty acids
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| sometimes called triglycerides, or fats/oils has a three carbon backbone (glycerol) + 3 fatty acids | Triacyglycerols
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| fx of Triacyglycerols | store energy; thermal insulation & padding
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| fat cells that are specialized with cytoplasm containing Triacyglycerols | Adip[ocytes
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| 2 fatty acids (non polar) + polar phosphate group + glycerol backbone | phospholipids
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| polar head and non polar tail making up phospholipids and glycolipids | amphipathic
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| found in abundance in membranes of myelinated cells composing the nervous system of HUMANS | glycolipids
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| 4 ringed structure. Include hormones, vitamin D and cholesterol | steroids
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| fx of steroid | important membrane component
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| included vitamin A ( vision vitamin) | terpenes
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| inhibitor of the synthesis of prostglandins | Aspirin
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| lipids are transported in the blood via | lipoprotein
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| major classes of lipoprotein | chylomicrons, VLDL, LDL,HDL
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| THE GREATER THE RATIO OF LIPID TO PROTEIN | THE LOWER THE DENSITY OF LIPOPROTEIN
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| 4 major fx of lipids | 1. structural (phospholipid) 2. store energy, provide insulation, paddying (triacyglycerols) 3. regulate metabolic activities (steroids) 4. serve as local hormones (eicosanoids)
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| chain of A.A. linked together by peptide bods | protein aka polypeptides
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| all species have the same | 20 alpha AA
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| Essential AA | humans have 10; body can NOT make these AA
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| Digested AA reach the cell in the form of | as single AA
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| number and sequence of AA | Primary structure
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| Alpha helix / Beta pleated sheets | Secondary structure
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| Parallel beta pleated sheets | two strands of the sheet lie in the SAME direction
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| Anti Parallel beta pleated sheets | two stands of the cell can lie in opposite directions
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| Hydrogen bonding occurs btwn carbonyl oxygen and hydrogen on the AMINE group | Alpha and Beta sheets bonding
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| conformation of protein | Secondary structure
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| T of F .....All proteins have a primary structure, some have a secondary and lager proteins have a tertiary and quantenary | TRUE
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| 3-D shape of a protein made when the peptide chain bends, culrs and folds | tertiary structure
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| 5 forces creatind the tertiary structure & quaternary structure:: | 1. covalent disulfide bonds btwn 2 cycteine AA on diff parts of the chain
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| " " | 2. elecrtostatic ( ionic) interactions mostly btwn acidic and basic side chains
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| " " | 3. hydrogen bonds
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| " " | 4. van der waals interactions
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| " " | 5. hydrophobic side chains pushed way from water ( toward center of the protein)
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| When 2 or more polypeptides chains bind together | Quaternary structure
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| when the conformation of a protein is disrupted | denatured
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| Carbohydrates (sugars/ sacharides) | Carbon + Water C(H2O)
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| Most common Carbs in nature : | pentose and hexose (glucose)
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| Carbs are delivered to the cell in the form of ? | glusoce which is made by the liver and entrocytes
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| 2 forms of the ring form of GLUCOSE | Anomers- 1. Alpha and 2. Beta glucose
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| Carb that has hydroxyl group on the anomeric carbon (C-1) and the methoxy group (C-6) on OPPOSITE sides of the carbon ring. | Alpha Glucose
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| Carb that has hydroxyl group on the anomeric carbon (C-1) and the methoxy group (C-6) on SAME sides of the carbon ring. | Beta Glucose
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| Animals eat the _____ linkages, but only bacteria can break the ____ linkages. | alpha; beta
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| if the cell has enough ATP, glucose is converted to ... | glycogen or fat cells for storage
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| Glycogen is made from | polymerization of glucose
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| structure of glycogen | branched glucose polymer with branched out alpha linkages
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| glycogen is found in | animal cells, esp. liver and muscle cells
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| T of F liver isone of the few cells that can convert glycogen back into glucose and release it back into the blood stream | TRUE
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| Which organ regulates blood glucose levels | liver
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| _____ & ______ can absorb glucose against a conc. gradient via Secondary Active Transport mechanism down con. gradient of Na+. | epithelial cells in the digestive tract ; epithelial cells in the proximal tubule of the kidney
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| Besides the epithelial cells in the digestive tract and proximal tubule, all other cells absorb glucose via | faciliated diffusion
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| ____ increases the rate of faciliated diffusion for glucose and other monosacharides | insulin
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| What 2 things do plants form from glucose? | 1. starch 2. Cellulose
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| 3 parts of a nucleotide | 1. Five Carbon Sugar 2. Nitrogenous Base 3. Phosphate group
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| sugar (pentose) + nitrogenous base | nuceoside
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| Polymers of nucleotides are: | DNA, RNA, Nucleic Acids, ATP, cAMP, NADH, & FADH2
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| nucleotides are joined together by : | phosphodiester bonds
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| 2 strands joined together by H- bonds to make a double helix | DNA
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| A and T | form 2 H- bonds
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| G and C | form 3 H-bonds
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| RNA | formed by one strand
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| NADH & FADH2 | coenzymes used in Kreb's cycle
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| Dissolved inorganic ions inside and outside the cell | Minerals
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| Minerals assist in ... | Transport of substances entering and exiting the cell by making a electrochemical gradient across the membrane
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| Minerals can... | combine and solidify to give strength to the matrix ( hydroxyapetite in bone)
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| Minerals act as cofactors by | assisting enzyme of protein function
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| what is the mineral found in heme (prosthetic group of cytochromes) | iron
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| if u see nitrogen think,,, | protein
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| Alpha and Beta linkages in polysasharides (carbs) are hydrolyzed by adding | water
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| T or F ...Enzyme catalysts can be reactants? | false
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| RNA | posseses a hydroxyl group at its 2nd pentose carbon atom
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| Some enzymes can be nucleic acids, but MOST are | GLOBULAR proteins
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| fx of enzyme | act as a catalyst----lowering Activation Energy & increasing rxn rate
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| Enzymes ( catalysts) are NEVER | consumed or permanently altered by any rxn
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| T or F ...Enzymes DO NOT alter the equilibrium of a rxn | TRUE
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| An example of enzyme specifictiy is ... | lock and key theory
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| lock and key theory ....the lock is the ___ and the key is the ___ | lock= active site of the enzyme; key= substrate
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| induced fit model | shape of both the enzyme and substrate are altered upon binding
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| Enzyme saturation kinetics | as conc. of substrate increases, rate of rxn also increases as well , but to a lesser degree untill the Vmax is reached
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| Enzymatic Rxns are affected by : | pH, temp, and substrate conc.
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| Km | good indicator of enzyme's affinity for it's substrate
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| Vmax | proportional to enzyme conc.
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| human body optimal temp... | 37 C
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| T or F.... optimal ph depends of the location of the enxyme | True
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| Pepsin | enzyme in stomach that prefers a pH of 2
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| Trypsin | enzyme in small intestine that prefers a pH of 6-7
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| non protein component of enzyme and can be coenzymes or metal ions | cofactor
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| T of F... Many coenzymes are vitamins of their derivatives | TRUE
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| Agents which bind covalently to enzymes and disrupt their fx | Irreversible inhibitors
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| An example of a toxic irreversible inhibitor is | pennicillin
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| Compete with the substrate by binding reversibly with non covalent bonds to the active site, therefore not allowing the substrate to bind for a few sec | Competitive inhibitors
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| Competitive ihibitors ____Vmax and ___Km | do not change; increase
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| Often resemble substrate | competitive inhibitors
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| Bind non covalently to an enzyme at a spot other than the active site and CHANGE the conformation of the enzyme. THEY DO NOT resemble the substrate , so they act on more than one enzyme.. | NON competitive inhibitors
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| T of F ...NON competitive inhibitors do prevent the substrate from binding? | FALSE... they DO NOT prevent
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| T of F... NON competitive inhibitors bind just as readily to enzymes that have a substrate as to those that don't | TRUE
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| NON COMP and COMP inhibitors differ by .. | NON COMP inhibitors CAN NOT be overcome by excess substrate
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| NON COMP inihibitors ___ Vmax and __Km | lower, do not change
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| Modification of the enzyme configuration resulting from the binding of an activator or inhibitor at a specific binding site on the enzyme... | Allosteric interactions/regulation
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| inihbits enzyme activity when a sufficient amount of product has been formed | negative feedback inhibition aka feedback inhibition
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| Feedback inhibiton does not resemble substrate...T or F | TRUE
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| FEEDback inhibition works by... | binding to the substrate and causing a conformational change
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| At LOW substrate conc... | small incr in substrate conc incr enzyme efficiency as well as reaction rate
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| first substrate changes the shape of the enzyme allowing other substrates to bind more easily | positive cooperativity
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| cooperativity inthe presence of the allosteric inihibitor 2,3 BPG | gives the oxygen dissociation curve of hemoglobin its sigmoidal shape ---Negative Cooperativity
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| suffix -ase , contain nitrogen ( so can be denatured) | ENZYMES
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| Delta G= | change in free energy for a rxn. Is the Diff. btwn reactants and products and is NOT changed by enzymes
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| Decrease temp of a rxn | Decrease rate of rxn
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| Lowering the conc of a substrate will | lower the rate of enzymatic activity if the enzyme is not saturated
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| Adding a non competitive inhibitor will | lower rate of rxn, b/c Vmax is lowered
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| Changing the pH will | increase or decrease rate of enzymatic rxn depending on the optimal pH
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| Comp inhibitors can be overcome by | adding more substrate
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| Glycolysis | takes a 6C sugar and breaks it down to 2 3C molecules ( pyruvate)
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| Products of glycolysis:: | 2 pyruvate, 2 ATP, 2 NADPH
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| Pyruvate | conjugate base of pyruvate acid
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| ATP | ADP + pi + water
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| NADHP | made from the reduction of NAD+
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| Glycolysis occurs in the _____ of the cell | CYTOSOL
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| Phosphate level phosphorylation in glycolysis | formation of ATP from ADP and pi using the energy released from the decay of high energy phophorylated compounds as opposed to using energy from diffusion
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| glycolysis uses... | 2 ATP...1) glucose --> glucose 6 phosphate 2) Fructose 6 phosphate--> fructose 1,6 biphophate
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| simple table sugar | dissachiride ( glucose + fructose)
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| Fructose & galactose | Monosachirides
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| lactose ( found in milk) | glucose + galactose
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| lactose is broken down in the ... | small intestine
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| Fermentation | anaerobic respiration
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| fermentation makes | lactic acid/ ethanol, NAD+, CO2 as a waste product
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| in fermentation... pyruvate is reduced into | ethanol OR lactic acid
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| in fermentation...NADPH is oxidized back to | NAD+ (which is used again in
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| Yeast produce | ethanol from fermentation
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| Human cells and other microorganisms produce | lactic acid from fermentation
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| Fermentation occurs if... | 1. A cell can not get the energy from NADPH and Pyruvate 2. No oxygen available
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| Aerobic Respiration occurs in the | mitochondrial matrix
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| Is the outer membrane of mitochondria is permeable to small molecules like | NADPH and pyruvate
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| NADPH and pyruvate pass through the outer membrane of the mitochondria via | faciliated diffusion through a large membrane protein called PORIN
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| Inner mitochondiral membrane= | less permeable
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| Pyruvate= converted to ____ in aerobic resp? | acetyl co A
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| Changing pyruvate into acetyl co A will produce | NADPH & CO2
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| Krebs cycle aka ? | Citric Acid Cycle
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| Each turn of the Krebs cycle produces ... | 1 ATP; 3 NADPH; 1 FADH2
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| Process of ATP production in Krebs Cycle= | substrate level phosphorylation
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| During the Kreb's cycle, 2 C are lost as? | CO2
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| What is reproduced in the Krebs cycle to start the cycle over again? | oxalacetate
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| Where are AA deaminated? | in the liver to make pyruvic acid or acetyl coA
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| Aerobic Respiration makes ____ ATP, including glycolysis | 36
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| 1 NADPH brings back ____ ATP | 2 or 3
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| 1 FADH2 brings back ___ ATP | 2
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| one glucose makes ____ turns of the kreb's cycle | 2
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| fatty acids and amino acids can be catabolized for energy via | Krebs cycle
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| A series of proteins, including cytochrome with HEME, in the inner membrane of the mitochondrion. | ETC
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| ETC | oxidizes NADPH, water is the final electron acceptor
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| in ETC, establishes a proton gradient from NADPH, which propels protons thru ATP Synthase to make ATP | Proton Motive Force
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| T or F...Intermembrane has a lower pH than the matrix | TRUE
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| Oxidative phosporylation | production of ATP from ETC through proton gradient; occurs in the mitochondria of the cell. In this process electrons are transferred from the oxidation of NADH+H+, and FADH2 to molecules of O2. This process requires O2 and is termed aeribic respiration.
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| Substrate level phosphoylation | production of ATP through glycolysis ( cytosol) & Krebs cycle (mitochondrial matrix) ; t removes a phosphate directly from a substrate and transfers it to ADP. This is accomplished anaerobically.
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| A KEY difference btwn Oxidative phosphorylation and Substrate level phosphorylation ... | Oxidative phosphorylation uses an electrochemical or chemiosmotic gradient of protons (H+) across the inner mitochondrial membrane to generate ATP from ADP
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| Respiration: is a combustion rxn | C6 H12 O6 + O2 --> CO2 + H2O
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| Net ATP of fermentation = | 2 ATP...which comes form glycolysis
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| ATP synthase | occurs part of ETC in the innner mitochondrial memebrane
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